I am continuing research on an estrogen binding protein, isolated from Candida albicans, known as EBP1. In the past year, I have begun to characterize the steady-state kinetic parameters of a model reaction this enzyme will catalyze, as well as UV-visual spectral changes that occur upon binding several ligands, including estradiol. The interpretation of this data has been greatly enhanced with the use of the Computer Graphics Lab and visualization of the crystal structure of a highly homologous enzyme, Old Yellow Enzyme. The orientation of various residues in the active site of this enzyme has allowed us to make more informed decisions about the way homologous residues in EBP may act to perform their function. Thus, these structural/mechanistic issues which form the basis of my research are much more easily examined in the context of structural models, available by use of the Computer Graphics Lab, and it continues to be an invaluable resource in my education and training.